DB code: T00219

CATH domain 3.40.50.720 : Rossmann fold
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 Catalytic domain
1.10.1870.10 : Domain 3, Saccharopine reductase
E.C. 1.5.1.10
CSA 1e5q
M-CSA 1e5q
MACiE

CATH domain Related DB codes (homologues)
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 D00003 D00010 D00017 D00023 D00027 D00028 D00034 D00476
3.40.50.720 : Rossmann fold S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q9P4R4 Saccharopine dehydrogenase {NADP+, L-glutamate-forming}
EC 1.5.1.10
Saccharopine reductase
XP_003716085.1 (Protein)
XM_003716037.1 (DNA/RNA sequence)
PF03435 (Saccharop_dh)
[Graphical View]

KEGG enzyme name
saccharopine dehydrogenase (NADP+, L-glutamate-forming)
saccharopine (nicotinamide adenine dinucleotide phosphate,glutamate-forming) dehydrogenase
aminoadipic semialdehyde-glutamic reductase
aminoadipate semialdehyde-glutamate reductase
aminoadipic semialdehyde-glutamate reductase
epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase(L-2-aminoadipate-semialdehyde forming)
saccharopine reductase
6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase(L-glutamate-forming)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q9P4R4 LYS9_MAGGR N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-glutamate + L-2-aminoadipate 6-semialdehyde + NADPH. Homodimer.

KEGG Pathways
Map code Pathways E.C.
MAP00300 Lysine biosynthesis
MAP00310 Lysine degradation

Compound table
Substrates Products Intermediates
KEGG-id C00005 C00025 C04076 C00080 C00006 C00449 C00001
E.C.
Compound NADPH L-Glutamate L-2-Aminoadipate 6-semialdehyde H+ NADP+ N6-(L-1,3-Dicarboxypropyl)-L-lysine H2O
Type amide group,amine group,nucleotide amino acids,carboxyl group amino acids,carbohydrate,lipid others amide group,amine group,nucleotide amino acids,amine group,carboxyl group H2O
ChEBI 16474
 16474
 		16015
 16015
 		17917
 58321
 17917
 58321
 		15378
 15378
 		18009
 18009
 		16927
 16927
 		15377
 15377
PubChem 5884
 5884
 		33032
 44272391
 88747398
 33032
 44272391
 88747398
 		160603
 36688062
 160603
 36688062
 		1038
 1038
 		5886
 5886
 		160556
 160556
 		22247451
 962
 22247451
 962
1e5lA01 Unbound Unbound Unbound Unbound Unbound
1e5lB01 Unbound Unbound Unbound Unbound Unbound
1e5qA01 Unbound Unbound Unbound Unbound Unbound
1e5qB01 Unbound Unbound Unbound Unbound Unbound
1e5qC01 Unbound Unbound Unbound Unbound Unbound
1e5qD01 Unbound Unbound Unbound Unbound Unbound
1e5qE01 Unbound Unbound Unbound Unbound Unbound
1e5qF01 Unbound Unbound Unbound Unbound Unbound
1e5qG01 Unbound Unbound Unbound Unbound Unbound
1e5qH01 Unbound Unbound Unbound Unbound Unbound
1ff9A01 Unbound Unbound Unbound Unbound Unbound
1e5lA02 Unbound Unbound Unbound Unbound Unbound
1e5lB02 Unbound Unbound Unbound Unbound Unbound
1e5qA02 Bound:NDP Unbound Unbound Unbound Bound:SHR
1e5qB02 Bound:NDP Unbound Unbound Unbound Bound:SHR
1e5qC02 Bound:NDP Unbound Unbound Unbound Bound:SHR
1e5qD02 Bound:NDP Unbound Unbound Unbound Bound:SHR
1e5qE02 Bound:NDP Unbound Unbound Unbound Bound:SHR
1e5qF02 Bound:NDP Unbound Unbound Unbound Bound:SHR
1e5qG02 Bound:NDP Unbound Unbound Unbound Bound:SHR
1e5qH02 Bound:NDP Unbound Unbound Unbound Bound:SHR
1ff9A02 Unbound Unbound Unbound Unbound Unbound
1e5lA03 Unbound Unbound Unbound Unbound Unbound
1e5lB03 Unbound Unbound Unbound Unbound Unbound
1e5qA03 Unbound Unbound Unbound Unbound Unbound
1e5qB03 Unbound Unbound Unbound Unbound Unbound
1e5qC03 Unbound Unbound Unbound Unbound Unbound
1e5qD03 Unbound Unbound Unbound Unbound Unbound
1e5qE03 Unbound Unbound Unbound Unbound Unbound
1e5qF03 Unbound Unbound Unbound Unbound Unbound
1e5qG03 Unbound Unbound Unbound Unbound Unbound
1e5qH03 Unbound Unbound Unbound Unbound Unbound
1ff9A03 Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1e5lA01
1e5lB01
1e5qA01
1e5qB01
1e5qC01
1e5qD01
1e5qE01
1e5qF01
1e5qG01
1e5qH01
1ff9A01
1e5lA02 ASP 126
1e5lB02 ASP 126
1e5qA02 ASP 126
1e5qB02 ASP 126
1e5qC02 ASP 126
1e5qD02 ASP 126
1e5qE02 ASP 126
1e5qF02 ASP 126
1e5qG02 ASP 126
1e5qH02 ASP 126
1ff9A02 ASP 126
1e5lA03
1e5lB03
1e5qA03
1e5qB03
1e5qC03
1e5qD03
1e5qE03
1e5qF03
1e5qG03
1e5qH03
1ff9A03

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Fig.7, p.1042-1044 3

References
[1]
Resource
Comments
Medline ID
PubMed ID 242268
Journal Arch Biochem Biophys
Year 1975
Volume 171
Pages 191-6
Authors Fjellstedt TA, Robinson JC
Title Properties of partially purified saccharopine dehydrogenase from human placenta.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 10587945
Journal Microb Comp Genomics
Year 1999
Volume 4
Pages 173-86
Authors Studley WK, Yamaguchi M, Hatefi Y, Saier MH Jr
Title Phylogenetic analyses of proton-translocating transhydrogenases.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11080625
Journal Structure Fold Des
Year 2000
Volume 8
Pages 1037-47
Authors Johansson E, Steffens JJ, Lindqvist Y, Schneider G
Title Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis.
Related PDB 1e5l 1e5q 1ffq
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 12393892
Journal J Biol Chem
Year 2002
Volume 277
Pages 49655-61
Authors Zhu X, Tang G, Galili G
Title The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains.
Related PDB
Related UniProtKB

Comments
Saccharopine Dehydrogenases are a collective term for the enzymes that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-lysine, or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-glutamate.
According to the paper [3], this enzyme catalyzes three different reactions, addition to double-bond, elimination accompanied by double-bond formation, and reduction.

Created Updated
2004-07-02 2009-02-26